Induction of cold shock proteins in Bacillus subtilis

Lottering, Eugene A.; Streips, Uldis N.

doi:10.1007/bf00293633

Cited by 47 publications

(42 citation statements)

References 25 publications

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“…(1) and the mesophile Lactococcus lactis subsp. lactis (37) or B. subtilis (29) had no lag phase consequent to a cold treatment. Their growth continued at an intermediate rate followed by a growth rate characteristic of final low temperature.…”

Section: Discussionmentioning

confidence: 95%

“…In the same way, this criterion of classification according to temperature range of growth fails to predict the consequences of cold shocks on protein synthesis. Indeed, after cold shock treatments, the relative rate of synthesis of most cellular proteins was maintained in P. fragi, as for other psychrotrophs such as B. psychrophilus (49) or A. globiformis (3), but also for mesophiles such as B. subtilis (29). On the contrary, the mesophile E. coli (18), but also the psychrotrophs L. monocytogenes and L. innocua (38), have a dramatic decrease in protein synthesis immediately after a downshift in temperature.…”

Section: Discussionmentioning

confidence: 99%

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The cold shock response of the psychrotrophic bacterium Pseudomonas fragi involves four low-molecular-mass nucleic acid-binding proteins

Michel¹,

Lehoux²,

Depret³

et al. 1997

J Bacteriol

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The psychrotrophic bacterium Pseudomonas fragi was subjected to cold shocks from 30 or 20 to 5°C. The downshifts were followed by a lag phase before growth resumed at a characteristic 5°C growth rate. The analysis of protein patterns by two-dimentional gel electrophoresis revealed overexpression of 25 or 17 proteins and underexpression of 12 proteins following the 30-or 20-to-5°C shift, respectively. The two downshifts shared similar variations of synthesis of 20 proteins. The kinetic analysis distinguished the induced proteins into cold shock proteins (Csps), which were rapidly but transiently overexpressed, and cold acclimation proteins (Caps), which were more or less rapidly induced but still overexpressed several hours after the downshifts. Among the cold-induced proteins, four low-molecular-mass proteins, two of them previously characterized as Caps (CapA and CapB), and heat acclimation proteins (Haps) as well as heat shock proteins (Hsps) for the two others (TapA and TapB) displayed higher levels of induction. Partial amino acid sequences, obtained by microsequencing, were used to design primers to amplify by PCR the four genes and then determine their nucleotide sequences. A BamHI-EcoRI restriction fragment of 1.9 kb, containing the complete coding sequence for capB, was cloned and sequenced. The four peptides belong to the family of small nucleic acid-binding proteins as CspA, the major Escherichia coli Csp. They are likely to play a major role in the adaptative response of P. fragi to environmental temperature changes.

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Section: Discussionmentioning

confidence: 95%

Section: Discussionmentioning

confidence: 99%

The cold shock response of the psychrotrophic bacterium Pseudomonas fragi involves four low-molecular-mass nucleic acid-binding proteins

Michel¹,

Lehoux²,

Depret³

et al. 1997

J Bacteriol

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“…About 60 proteins of B. subtilis have been identified on 2-D polyacrylamide gels so far (see also Graumann et al, 1996;Lottering & Streips, 1995 ;Miller et al, 1991 ;Schmid et al, 1997;H. Antelmann and others, unpublished).…”

Section: Discussionmentioning

confidence: 99%

Specific and general stress proteins in Bacillus subtilis � a two-dimensional protein electrophoresis study

et al. 1997

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A computer-aided analysis of high resolution two-dimensional polyacrylamide gels was used to investigate the changes in the protein synthesis profile in B. subtilis wild-type strains and sigB mutants in response to heat shock, salt and ethanol stress, and glucose or phosphate starvation. The data provided evidence that the induction of a t least 42 general stress proteins absolutely required the alternative sigma factor oB. However, a t least seven stress proteins, among them ClpC, ClpP, Sod, AhpC and AhpF, remained stressinducible in a sigB mutant. Such a detailed analysis also permitted the description of subgroups of general stress proteins which are subject to additional regulatory circuits, indicating a very thorough fine-tuning of this complex response. The relative synthesis rate of the general stress proteins constituted up to 40% of the total protein synthesis of stressed cells and thereby emphasizes the importance of the stress regulon. Besides the induction of these general or rather unspecific stress proteins, the induction of stress-specif ic proteins is shown and discussed.

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“…Although synthesis of the majority of proteins decreases after a temperature downshift, the level of a specific group of proteins increases under these conditions in B. subtilis (Lottering & Streips, 1995 ;Graumann et al, 1996). Using two-dimensional (2D) protein gel electrophoresis, it has been demonstrated that the synthesis of at least 37 proteins of B. subtilis increases after a temperature shift from 37 to 15 mC (Graumann et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

Genome-wide transcriptional profiling of the Bacillus subtilis cold-shock response

et al. 2002

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The transcriptome of Bacillus subtilis was analysed at different time points (30, 60 and 90 min) after a temperature downshift from 37 to 18 SC using DNA macroarrays. This approach allowed the identification of around 50 genes exhibiting an increased mRNA level and around 50 genes exhibiting a decreased mRNA level under cold-shock conditions. Many of the repressed genes encode enzymes involved in the biosynthesis of amino acids, nucleotides and coenzymes, indicating metabolic adaptation of the cells to the decreased growth rate at the lower temperature. The strongest cold-inducible gene encodes fatty acid desaturase, which forms unsaturated fatty acids from saturated phospholipid precursors, thereby increasing membrane fluidity. The cold-shock-induced increase of mRNA levels of the classical cold-shock genes cspB, cspC and cspD could be verified. Furthermore, besides many genes encoding proteins of unknown function, some genes encoding ribosomal proteins were transcriptionally up-regulated, which points to an adaptive reprogramming of the ribosomes under cold-shock conditions. Interestingly, the amount of mRNA specified by the operon ptb-bcd-buk-lpd-bkdA1-bkdA2-bkdB, which encodes enzymes involved in degradation of branched-chain amino acids, also increases after a temperature downshift. As cells utilize the isoleucine and valine degradation intermediates α-methylbutyryl-CoA and isobutyryl-CoA for synthesis of branched-chain fatty acids, this finding reflects the adaptation of membrane lipid composition, ensuring the maintenance of appropriate membrane fluidity at low temperatures. The results of the DNA array analyses were verified for several selected genes by RNA slot-blot analysis and compared with two-dimensional PAGE analyses.

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Induction of cold shock proteins in Bacillus subtilis

Cited by 47 publications

References 25 publications

The cold shock response of the psychrotrophic bacterium Pseudomonas fragi involves four low-molecular-mass nucleic acid-binding proteins

The cold shock response of the psychrotrophic bacterium Pseudomonas fragi involves four low-molecular-mass nucleic acid-binding proteins

Specific and general stress proteins in Bacillus subtilis � a two-dimensional protein electrophoresis study

Genome-wide transcriptional profiling of the Bacillus subtilis cold-shock response

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